Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

---

Query: EC:3.1.3.1 (alkaline phosphatase)
47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Venous blood values were determined on 19 Southdown sheep (9 adult ewes and 10 wether lambs). Principal sheep were given 12.5 ml of 3.3M urea solution/kg of body weight, which produced acute ammonia toxicosis. Whole blood ammonium-nitrogen was determined by ion exchange; venous blood gases and pH were measured with a pH blood gas analyzer; and 23 serum chemical analyses were obtained with a sequential multiple autoanalyzer computer. Analysis of variance for the data revealed significant changes for 20 values. The values are presented and discussed with regard to those that changed beyond acceptable limits (whole blood ammonium-nitrogen, venous blood pH, serum glucose, serum lactate dehydrogenase, serum alkaline phosphatase, serum creatine kinase, serum urea nitrogen, serum inorganic phosphorus, serum sodium, and serum potassium), those that changed within acceptable limits (PVo2, PVco2, serum triglycerides, serum free fatty acids, plasma volatile fatty acids, serum aspartate aminotransferase, serum total protein, serum albumin, serum creatinine, urea nitrogen-creatinine ratio, serum uric acid, serum cholesterol, serum low-density lipoproteins, serum calcium, serum iron and serum chloride), and those with no change (total and direct serum bilirubin and albumin-globulin ratio). Metabolic consequences of ammonia toxicosis are considered with regard to energy, lipid , protein, and acid-base and electrolyte balances. Blood values having possible laboratory diagnosis value and considerations for therapeutic adjustment are discussed.
...
PMID:Ovine blood chemistry values measured during ammonia toxicosis. 710 77

Alkaline phosphatase has been purified from microsomes of chicken epiphyseal cartilage by first selectively extracting certain adventitious proteins with 0.25 M trichloroacetate. The membrane-bound enzyme was then solubilized by 1% cholate in buffered 33% saturated ammonium sulfate and purified by column chromatography on Bio-Gel A-5m, extraction with 1-butanol, and ion exchange chromatography on DEAE-Bio-Gel A. The purified alkaline phosphatase from the cartilage membrane had a subunit molecular weight of 53,000 and a holoenzyme weight of 207,000-220,000, indicating a tetramer. The pH optima for p-nitrophenylphosphate, ATP, and pyrophosphate hydrolysis were 10.3, 9.0, and 8.5, respectively. Values of Vmax (in micromoles/min/mg) were 220, 3.1, and 0.8, respectively. Substrate inhibition was pronounced at values of pH below 8.5. Inhibition of p-nitrophenylphosphate hydrolysis at pH 10.3 showed that phosphate and arsenate were competitive inhibitors (KI = 1.88 and 0.15 mM, respectively) and levamisole was an uncompetitive inhibitor (KI = 0.32 mM), while L-phenylalanine and ZnCl2 were mixed inhibitors (KI = 15.8 and 0.02 mM, respectively). Inhibition by preincubation in 1 mM EDTA was reversible by readdition of 0.25 mM MgCl2 nd 20 microM ZnCl2. The data indicate that this membrane-bound alkaline phosphatase from chicken epiphyseal cartilage is a Zn2+ and possibly Mg2+-containing enzyme. While the subunit molecular weight and kinetic properties of the enzyme are quite typical of vertebrate alkaline phosphatases, the tightness of binding to the membrane lipids, the extreme sensitivity to substrate inhibition, and the tetrameric conformation of the holoenzyme are unusual.
...
PMID:Purification and initial characterization of intrinsic membrane-bound alkaline phosphatase from chicken epiphyseal cartilage. 725 97

We describe a method for determining serum alkaline phosphatase activity with use of N-methyl-D-glucamine buffer, Na+ is a definite activator, whereas NH4+ and Li+ inhibit enzyme activity. Optimum reaction conditions are: methylglucamine buffer, 0.35 mol/L, pH 10.2 +/- 0.1 (30 degrees C); NaCl, 70 mmol/L; MgCl2, 0.5 mmol/L; disodium 4-nitrophenyl phosphate, 15 mmol/L; reaction temperature, 30 degrees C; reaction time, 2 min. The assay conditions are optimum for all human serum isoenzymes.
...
PMID:Use of N-methyl-D-glucamine as buffer in the determination of serum alkaline phosphatase activity. 728 25

Chronic oral administration of ammonium molybdate in rats markedly retarded the growth rate of rats and high protein diet could partially reverse this condition. The activities of several enzymes viz. acid phosphatase, alkaline phosphatase, glucose-6-phosphatase, succinic dehydrogenase, glutamate oxaloacetate transaminase, inorganic pyrophosphatase and acetylcholinesterase in different tissues and serum levels of luteinizing hormone, follicle stimulating hormone, prolactin and cortisol are altered due to the toxicity conditions and high protein diet fed group of animals showed almost normal values in respect of a few of these parameters. Normal histological pattern of both liver and kidney tissues were altered under molybdenum toxicity condition. Significant increase of basophilic substances are observed in the cytoplasm of the liver cells of the toxic group of animals which is counteracted by feeding high protein diet.
...
PMID:Biochemical studies on molybdenum toxicity in rats: effects of high protein feeding. 732 62

DNases A1 and A2 have been purified to homogeneity from the hepatopancreas of Achatina fulica by a series of steps: acetate buffer extraction, ammonium sulfate precipitation and column chromatography on hydroxylapatite, phosphocellulose, Blue-Sepharose, and poly(A)-Sepharose. The purified enzymes are free of acidic phosphomonoesterase, phosphodiesterase, and RNase activities. They are slightly acidic glycoproteins with identical isoelectric point (6.90). On 0.1% SDS gel electrophoresis, DNase A2 had a molecular weight of 30,000 when dissolved in 1% SDS, but it had molecular weights of 17,500, 8,000, and 4,800 when dissolved in 1% SDS and 1% 2-mercaptoethanol. This was evidence that the enzyme consists of three different subunits joined by interchain disulfide bonds. DNases A1 and A2 are endonucleases working at acidic pH (3.5--6.0) and do not require divalent cations for their activities. The enzymes degrade poly(dA) 5 times faster and poly(dT) 3 times faster than heat-denatured DNA under optimal conditions but do not appreciably digest poly(dG) and poly(dC). We developed an analytical procedure for oligodeoxynucleotides by high-performance liquid chromatography. The phosphomonoester end group and the mode of degradation were examined by the method. The termini produced by the enzymes have 3'-phosphoryl and 5'-hydroxy end groups. The products of exhaustive hydrolysis contain di-, tri-, tetra-, and pentanucleotides and mononucleotide was barely detected. The hydrolyzing activities of DNases A1 and A2 are stimulated by polyamines such as spermine, spermidine, and putrescine, but are inhibited by synthetic polynucleotides and various drugs. Adenosine deaminase highly active on oligoadenylic acids was found in a crude DNase A fraction. The enzyme preparation has higher activity on 3'-adenylic acid than on 5'-adenylic acid. The first adenosine residue of oligoadenylic acids was deaminated considerably more rapidly than the second or succeeding ones.
...
PMID:DNase A, a poly(dA) and poly(dT)-specific deoxyribonuclease from Achatina fulica. Purification and characterization. 733 15

The effects of zinc pyrithione (ZnPT) and sodium pyrithione (NaPT), including the influence of various vehicles, upon whole blood and plasma zinc levels and serum alkaline phosphatase (SAP) have been investigated in rabbits following dermal and/or iv administration. Two such vehicles, ammonium lauryl sulfate (ALS) and triethanolamine lauryl sulfate, affected zinc homeostasis differently than the pyrithiones, in that, unlike the pyrithiones, no whole blood changes were observed, although there were delayed and sustained declines in plasma zinc and SAP values. These changes were most likely related to the skin irritation caused by the surfactants. In contrast, NaPT-dimethyl sulfoxide (DMSO) dermal and iv exposures produced rapid decreases in plasma zinc followed by quick recovery, coupled with smaller and unsustained declines in SAP. Large increases in whole blood zinc were also observed in both cases, as well as in a ZnPT-DMSO iv exposure. DMSO itself had no effects on the measured parameters. Experiments involving combinations of the pyrithiones and ALS demonstrated effects on zinc homeostasis that were attributable to both substances, i.e. large increases in whole blood zinc (PT effect), quick drops in plasma zinc (PT effect) and slowly recovering plasma zinc and SAP values (surfactant effect). The chelating nature of the PT molecule may have been responsible for some of the observed changes in zinc distribution.
...
PMID:Effects of pyrithiones and surfactants on zinc and enzyme levels in rabbits. 739 40

An improved procedure for the purification of alkaline phosphatase from about 10 g of day 7 pregnant mouse uterine tissue is described. Following homogenization, the procedure involved solubilization and extraction with 0.8% (v/v) Triton X-100 and 20% (v/v) n-butanol, ammonium sulfate precipitation, concanavalin A-Sepharose 4B affinity chromatography, DEAE-cellulose anion-exchange chromatography and Sephacryl S200 gel filtration. On subjecting 2162-fold purified enzyme preparations to polyacrylamide-gel electrophoresis, a single band of protein coincident with the zone of enzyme activity and having an apparent molecular weight of 205 000 +/- 10 000 was identified. Affinity chromatography yielded the largest increase in purity of any step in the procedure and established the glycoprotein nature of the uterine enzyme. Some metalloenzyme properties of the phosphatase were also studied and it was demonstrated that both Mg2+ and Zn2+ ions are necessary for hydrolytic activity. Treatment with neuraminidases retarded the anodal migration of the enzyme during electrophoresis on cellulose acetate membranes but did not influence its activity or catalytic properties. These results suggest that the uterine alkaline phosphatase is a sialoglycoprotein. The sialic acid residues, however, do not appear to constitute part of the active centre of the enzyme. In addition, the optimum pH for activity depended on substrate concentration and decreased with decreasing substrate concentration. Apparent Km values also depended on variations in pH and decreased with decreasing pH. Plots of pKm versus pH revealed a functional group with a pK value of 9.45. The enzyme also hydrolysed a variety of compounds having either phosphomonoester or pyrophosphate linkages and was inactivated after heating at 60 degrees C for 15 min. The activation energy, determined from a linear Arrhenius plot, was 50.1 kJ mol-1.
...
PMID:Mouse uterine alkaline phosphatase: improved purification by affinity chromatography and further characterization of the enzyme. 742 65

Feasibility for the structural characterization of modified nucleosides in transfer RNA at low microgram levels has been investigated by using continuous-flow frit-fast atom bombardment liquid chromatography/mass spectrometry (frit-FAB LC/MS). Sample of tRNA(Phe) from brewer's yeast (Saccharomyces cerevisiae) was used as a main model, and enzymatically hydrolysed by nuclease P1 and alkaline phosphatase. The resulting nucleoside mixture was separated by using a microbore reversed-phase LC column (150 mm x 0.5 mm i.d.) with an aqueous ammonium acetate-methanol gradient, and the mass spectra were acquired on both positive and negative ionization modes. The modified nucleosides were characterized by comparison of the relative LC elution times with authentic nucleosides, and further confirmed by the structural information from the frit-FAB mass spectra where both molecular and base ions were in general observed as intense peaks in both ionization modes. Typically, 0.06-0.2 A260 units (3-10 micrograms) of isoaccepting tRNA was enough to obtain full-scan mass spectra of modified nucleosides, often occurring at a frequency of one per tRNA molecule using positive ion detection. The LC/MS system was used to screen modified nucleosides in tRNA of the extremely thermophilic microorganism Pyrodictium occultum.
...
PMID:Structural characterization of modified nucleosides in tRNA hydrolysates by frit-fast atom bombardment liquid chromatography/mass spectrometry. 752 77

PKN, a novel protein kinase with a catalytic domain homologous to that of the protein kinase C (PKC) family and unique N-terminal leucine-zipper-like sequences, was identified by molecular cloning from a human hippocampus cDNA library [Mukai and Ono (1994) Biochem. Biophys. Res. Commun. 199, 897-904]. Recently we partially purified recombinant PKN from COS7 cells transfected with the cDNA construct encoding human PKN, and demonstrated that the recombinant PKN was activated by unsaturated fatty acids and limited proteolysis [Mukai, Kitagawa, Shibata et al. (1994) Biochem. Biophys. Res. Commun. 204, 348-356]. The present work has focused on the further purification and characterization of PKN from native rat tissue. Immunochemical measurement revealed that PKN was found in every tissue, and was especially abundant in testis, spleen and brain; subcellular fractionation of rat brain showed that half of the PKN was localized in the soluble cytosolic fraction. PKN was purified approx. 8000-fold to apparent homogeneity from the cytosolic fraction of rat testis by DEAE-cellulose chromatography, ammonium sulphate fractionation and chromatography on butyl-Sepharose, heparin-Sepharose, Mono Q and protamine-CH-Sepharose. The enzyme migrates as a band of apparent molecular mass 120 kDa. Using serine-containing peptides based on the pseudosubstrate sequence of PKC-delta as phosphate acceptors, the kinase activity was stimulated several-fold by 40 microM unsaturated fatty acids or by detergents such as 0.04% sodium deoxycholate and 0.004% SDS. In the absence of modifiers, protamine sulphate, myelin basic protein and synthetic peptides based on the pseudosubstrate site of PKCs or ribosomal S6 protein were good substrates for phosphorylation by the kinase. In the presence of 40 microM arachidonic acid the kinase activity of PKN for these phosphate acceptors was increased 2-18-fold. The autophosphorylation activity of purified PKN was partially inhibited by pretreatment with alkaline phosphatase. These properties appear to distinguish PKN from many protein kinases isolated previously.
...
PMID:Purification and characterization of a fatty acid-activated protein kinase (PKN) from rat testis. 765 8

A soil incubation experiment was carried out in a complex experimental system to simulate the effect of environmental factors and 3 trace elements on the phosphomonoesterase and amidase activity of 2 soils. DISITOBI model assures information about experimental object characterized by multidimensional response-function. Plant residue+mineral nitrogen addition increased phosphomonoesterase activity of investigated soils through its effect on enzyme synthesis. A significant part of the increase in phosphomonoesterase activity is the result of the exogenous enzyme input of plant residues. Mineral phosphorus addition reduced the activity after 16 days incubation under our experimental conditions. Plant residue+mineral nitrogen addition reduced amidase activity of chernozem soil presumably due to ammonium and nitrate inhibiting soil amidases.
...
PMID:Effects of environmental factors and Mn, Zn, Cu trace elements on the soil phosphomonoesterase and amidase activity. Application of DISITOBI model. 774 Aug 99


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>

---